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P25374

- NFS1_YEAST

UniProt

P25374 - NFS1_YEAST

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Protein

Cysteine desulfurase, mitochondrial

Gene

NFS1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Catalyzes the removal of elemental sulfur from cysteine to produce alanine. It supplies the inorganic sulfur for iron-sulfur (Fe-S) clusters. Involved in both tRNA-processing and mitochondrial metabolism.

Catalytic activityi

L-cysteine + acceptor = L-alanine + S-sulfanyl-acceptor.

Cofactori

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei421 – 4211By similarity

GO - Molecular functioni

  1. cysteine desulfurase activity Source: SGD
  2. pyridoxal phosphate binding Source: InterPro

GO - Biological processi

  1. cellular iron ion homeostasis Source: SGD
  2. cysteine metabolic process Source: InterPro
  3. iron-sulfur cluster assembly Source: SGD
  4. mitochondrial tRNA thio-modification Source: SGD
  5. tRNA thio-modification Source: SGD
  6. tRNA wobble uridine modification Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

tRNA processing

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

BioCyciMetaCyc:G3O-29283-MONOMER.
YEAST:G3O-29283-MONOMER.
ReactomeiREACT_189017. Mitochondrial iron-sulfur cluster biogenesis.
REACT_189051. Molybdenum cofactor biosynthesis.

Names & Taxonomyi

Protein namesi
Recommended name:
Cysteine desulfurase, mitochondrial (EC:2.8.1.7)
Alternative name(s):
tRNA-splicing protein SPL1
Gene namesi
Name:NFS1
Synonyms:SPL1
Ordered Locus Names:YCL017C
ORF Names:YCL17C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome III

Organism-specific databases

CYGDiYCL017c.
SGDiS000000522. NFS1.

Subcellular locationi

GO - Cellular componenti

  1. L-cysteine desulfurase complex Source: SGD
  2. mitochondrion Source: SGD
  3. nucleus Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3333MitochondrionSequence AnalysisAdd
BLAST
Chaini34 – 497464Cysteine desulfurase, mitochondrialPRO_0000001304Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei299 – 2991N6-(pyridoxal phosphate)lysineBy similarity

Proteomic databases

MaxQBiP25374.
PaxDbiP25374.
PeptideAtlasiP25374.
PRIDEiP25374.

Expressioni

Gene expression databases

GenevestigatoriP25374.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
ISD11Q6Q56010EBI-11991,EBI-784315
ISU1Q030202EBI-11991,EBI-29901

Protein-protein interaction databases

BioGridi30967. 20 interactions.
DIPiDIP-2948N.
IntActiP25374. 14 interactions.
MINTiMINT-474525.
STRINGi4932.YCL017C.

Structurei

3D structure databases

ProteinModelPortaliP25374.
SMRiP25374. Positions 99-491.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG1104.
GeneTreeiENSGT00530000063513.
HOGENOMiHOG000017510.
InParanoidiP25374.
KOiK04487.
OMAiVDYTVQK.
OrthoDBiEOG7ZKSMC.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProiIPR000192. Aminotrans_V_dom.
IPR020578. Aminotrans_V_PyrdxlP_BS.
IPR010240. Cys_deSase.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PfamiPF00266. Aminotran_5. 1 hit.
[Graphical view]
SUPFAMiSSF53383. SSF53383. 1 hit.
TIGRFAMsiTIGR02006. IscS. 1 hit.
PROSITEiPS00595. AA_TRANSFER_CLASS_5. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P25374-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MLKSTATRSI TRLSQVYNVP AATYRACLVS RRFYSPPAAG VKLDDNFSLE
60 70 80 90 100
THTDIQAAAK AQASARASAS GTTPDAVVAS GSTAMSHAYQ ENTGFGTRPI
110 120 130 140 150
YLDMQATTPT DPRVLDTMLK FYTGLYGNPH SNTHSYGWET NTAVENARAH
160 170 180 190 200
VAKMINADPK EIIFTSGATE SNNMVLKGVP RFYKKTKKHI ITTRTEHKCV
210 220 230 240 250
LEAARAMMKE GFEVTFLNVD DQGLIDLKEL EDAIRPDTCL VSVMAVNNEI
260 270 280 290 300
GVIQPIKEIG AICRKNKIYF HTDAAQAYGK IHIDVNEMNI DLLSISSHKI
310 320 330 340 350
YGPKGIGAIY VRRRPRVRLE PLLSGGGQER GLRSGTLAPP LVAGFGEAAR
360 370 380 390 400
LMKKEFDNDQ AHIKRLSDKL VKGLLSAEHT TLNGSPDHRY PGCVNVSFAY
410 420 430 440 450
VEGESLLMAL RDIALSSGSA CTSASLEPSY VLHALGKDDA LAHSSIRFGI
460 470 480 490
GRFSTEEEVD YVVKAVSDRV KFLRELSPLW EMVQEGIDLN SIKWSGH
Length:497
Mass (Da):54,467
Last modified:March 15, 2004 - v2
Checksum:iD709E326B3921BCC
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti150 – 1501H → Y in AAA34814. (PubMed:8444805)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M98808 Genomic DNA. Translation: AAA34814.1.
X59720 Genomic DNA. Translation: CAA42344.2.
M12909 Genomic DNA. Translation: AAA66918.1.
BK006937 Genomic DNA. Translation: DAA07466.1.
PIRiS19343.
RefSeqiNP_009912.2. NM_001178664.1.

Genome annotation databases

EnsemblFungiiYCL017C; YCL017C; YCL017C.
GeneIDi850343.
KEGGisce:YCL017C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M98808 Genomic DNA. Translation: AAA34814.1 .
X59720 Genomic DNA. Translation: CAA42344.2 .
M12909 Genomic DNA. Translation: AAA66918.1 .
BK006937 Genomic DNA. Translation: DAA07466.1 .
PIRi S19343.
RefSeqi NP_009912.2. NM_001178664.1.

3D structure databases

ProteinModelPortali P25374.
SMRi P25374. Positions 99-491.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 30967. 20 interactions.
DIPi DIP-2948N.
IntActi P25374. 14 interactions.
MINTi MINT-474525.
STRINGi 4932.YCL017C.

Proteomic databases

MaxQBi P25374.
PaxDbi P25374.
PeptideAtlasi P25374.
PRIDEi P25374.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YCL017C ; YCL017C ; YCL017C .
GeneIDi 850343.
KEGGi sce:YCL017C.

Organism-specific databases

CYGDi YCL017c.
SGDi S000000522. NFS1.

Phylogenomic databases

eggNOGi COG1104.
GeneTreei ENSGT00530000063513.
HOGENOMi HOG000017510.
InParanoidi P25374.
KOi K04487.
OMAi VDYTVQK.
OrthoDBi EOG7ZKSMC.

Enzyme and pathway databases

BioCyci MetaCyc:G3O-29283-MONOMER.
YEAST:G3O-29283-MONOMER.
Reactomei REACT_189017. Mitochondrial iron-sulfur cluster biogenesis.
REACT_189051. Molybdenum cofactor biosynthesis.

Miscellaneous databases

NextBioi 965791.
PROi P25374.

Gene expression databases

Genevestigatori P25374.

Family and domain databases

Gene3Di 3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProi IPR000192. Aminotrans_V_dom.
IPR020578. Aminotrans_V_PyrdxlP_BS.
IPR010240. Cys_deSase.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view ]
Pfami PF00266. Aminotran_5. 1 hit.
[Graphical view ]
SUPFAMi SSF53383. SSF53383. 1 hit.
TIGRFAMsi TIGR02006. IscS. 1 hit.
PROSITEi PS00595. AA_TRANSFER_CLASS_5. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "SPL1-1, a Saccharomyces cerevisiae mutation affecting tRNA splicing."
    Leong-Morgenthaler P.M., Kolman C., Oliver S.G., Hottinger H., Soell D.
    J. Bacteriol. 175:1433-1442(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The complete DNA sequence of yeast chromosome III."
    Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M., Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G., Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A., Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M.
    , Carcano C., Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M., Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C., Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M., Fabre F., Fairhead C., Faye G., Feldmann H., Fiers W., Francingues-Gaillard M.-C., Franco L., Frontali L., Fukuhara H., Fuller L.J., Galland P., Gent M.E., Gigot D., Gilliquet V., Glansdorff N., Goffeau A., Grenson M., Grisanti P., Grivell L.A., de Haan M., Haasemann M., Hatat D., Hoenicka J., Hegemann J.H., Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P., Huse K., Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M., Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P., Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G., Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E., Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F., Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L., Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J., Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B., Pohl F.M., Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A., Remacha M.A., Richterich P., Roberts A.B., Rodriguez F., Sanz E., Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y., Skala J., Slonimski P.P., Sor F., Soustelle C., Spiegelberg R., Stateva L.I., Steensma H.Y., Steiner S., Thierry A., Thireos G., Tzermia M., Urrestarazu L.A., Valle G., Vetter I., van Vliet-Reedijk J.C., Voet M., Volckaert G., Vreken P., Wang H., Warmington J.R., von Wettstein D., Wicksteed B.L., Wilson C., Wurst H., Xu G., Yoshikawa A., Zimmermann F.K., Sgouros J.G.
    Nature 357:38-46(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Valles G., Volckaerts G.
    Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION TO 150.
  4. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. "Nucleotide sequence of the 3' terminal region of the LEU2 gene from Saccharomyces cerevisiae."
    Froman B.E., Tait R.C., Rodriguez R.L.
    Gene 31:257-261(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 459-497.
  6. "The mitochondrial proteins Atm1p and Nfs1p are essential for biogenesis of cytosolic Fe/S proteins."
    Kispal G., Csere P., Prohl C., Lill R.
    EMBO J. 18:3981-3989(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  7. "Yeast mitochondrial protein, Nfs1p, coordinately regulates iron-sulfur cluster proteins, cellular iron uptake, and iron distribution."
    Li J., Kogan M., Knight S.A., Pain D., Dancis A.
    J. Biol. Chem. 274:33025-33034(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  8. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiNFS1_YEAST
AccessioniPrimary (citable) accession number: P25374
Secondary accession number(s): D6VQZ7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: March 15, 2004
Last modified: November 26, 2014
This is version 132 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 504 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome III
    Yeast (Saccharomyces cerevisiae) chromosome III: entries and gene names

External Data

Dasty 3